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An Improved Test Method for Assaying the Inhibition of Bioflavonoids on Xanthine Oxidase Activity in vitro.
Yao, Yuanyong; Wu, Tao; Zhang, Meng; Fu, Daihua; Yang, Hai; Chen, Shixue.
Afiliação
  • Yao Y; State Ethnic Affairs Commission Key Development Laboratory of Chinese Veterinary Medicine & National and Local Joint Engineering Center of Chinese Veterinary Medicine Separation and Purification Technology, Tongren Vocational and Technical University, Tongren, 554300, China.
  • Wu T; Institute of Material and Chemical Engineering, Tongren University, Tongren, 554300, China.
  • Zhang M; Institute of Material and Chemical Engineering, Tongren University, Tongren, 554300, China.
  • Fu D; Institute of Material and Chemical Engineering, Tongren University, Tongren, 554300, China.
  • Yang H; Institute of Material and Chemical Engineering, Tongren University, Tongren, 554300, China.
  • Chen S; Key Laboratory of Medicinal Chemistry for Natural Resource of Ministry of Education, Yunnan University, Kunming, 650091, China.
ChemistryOpen ; : e202400127, 2024 Sep 09.
Article em En | MEDLINE | ID: mdl-39246250
ABSTRACT
The difference on inhibitory effects of bioflavonoids inhibiting XOD activity assayed by varying test methods cause of us to be further in consideration. The reported test method creating a micro-environment surrounding XOD in the absence of ⋅O2 -, which is seemly different from the assay in vivo. So, the vitro test method for assaying XOD activity is necessary to be improved for selection of potential inhibitors in the presence of ⋅O2 -. The inhibitory results demonstrated that bioflavonoids of MY, DMY, QUE and LUT are capable to be on effective IC50 values, but others are not. As well, their resulting inhibitions determined by the improved test method are much less than that reported in the literature, indicating that their chemical affinities with XOD become weaker. Moreover, DMY assayed on the inhibitions of XOD in the improved test method performs to be a better inhibitor, as compared to the assay of the reported test methods. Abasing on the transformation of DMY into MY in the presence of ⋅O2 -, the good inhibition of DMY on XOD activity can be explained by the synergistic effect of MY.
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Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2024 Tipo de documento: Article